| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Trigo. |
|
Data corrente: |
26/08/2019 |
|
Data da última atualização: |
26/08/2019 |
|
Tipo da produção científica: |
Resumo em Anais de Congresso |
|
Autoria: |
MIRANDA, M. Z. de; TATSCH, P. O.; GUARIENTI, E. M.; BASSOI, M. C.; SÓ E SILVA, M.; SOARES SOBRINHO, J.; MACIEL, J. L. N.; FRONZA, V.; SCHEEREN, P. L. |
|
Afiliação: |
MARTHA ZAVARIZ DE MIRANDA, CNPT; PIHETRA OLIVEIRA TATSCH, CNPT; ELIANA MARIA GUARIENTI, CNPT; MANOEL CARLOS BASSOI, CNPSO; MARCIO SÓ E SILVA; JOAQUIM SOARES SOBRINHO, CNPT; JOAO LEODATO NUNES MACIEL, CNPT; VANOLI FRONZA, CNPT; PEDRO LUIZ SCHEEREN, CNPT. |
|
Título: |
Relationship between rapid flour check method and traditional analyses for wheat gluten quality evaluation to brazilian wheat genotypes: a preliminary study. |
|
Ano de publicação: |
2019 |
|
Fonte/Imprenta: |
In: INTERNATIONAL WHEAT CONGRESS, 1., 2019, Saskatoon, SK, Canada. Abstracts, proceedings, poster presentations... Saskatoon: University of Saskatchewan, 2019. Trab. 020301, p. 225. |
|
Idioma: |
Inglês |
|
Thesagro: |
Farinha de Trigo; Glúten; Seleção Fenótipa. |
|
Thesaurus Nal: |
Phenotype; Wheat flour; Wheat gluten. |
|
Categoria do assunto: |
G Melhoramento Genético |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/201322/1/ID44662-2019IWCposterp225.pdf
|
|
Marc: |
LEADER 00986nam a2200265 a 4500
001 2111642
005 2019-08-26
008 2019 bl uuuu u00u1 u #d
100 1 $aMIRANDA, M. Z. de
245 $aRelationship between rapid flour check method and traditional analyses for wheat gluten quality evaluation to brazilian wheat genotypes$ba preliminary study.$h[electronic resource]
260 $aIn: INTERNATIONAL WHEAT CONGRESS, 1., 2019, Saskatoon, SK, Canada. Abstracts, proceedings, poster presentations... Saskatoon: University of Saskatchewan, 2019. Trab. 020301, p. 225.$c2019
650 $aPhenotype
650 $aWheat flour
650 $aWheat gluten
650 $aFarinha de Trigo
650 $aGlúten
650 $aSeleção Fenótipa
700 1 $aTATSCH, P. O.
700 1 $aGUARIENTI, E. M.
700 1 $aBASSOI, M. C.
700 1 $aSÓ E SILVA, M.
700 1 $aSOARES SOBRINHO, J.
700 1 $aMACIEL, J. L. N.
700 1 $aFRONZA, V.
700 1 $aSCHEEREN, P. L.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Trigo (CNPT) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
Registro Completo
|
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
|
Data corrente: |
23/01/2012 |
|
Data da última atualização: |
24/02/2023 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Circulação/Nível: |
A - 2 |
|
Autoria: |
MULINARI, F.; BECKER-RITT, A. B.; DEMARTINI, D. R.; LIGABUE-BRAUN, R.; STANISÇUASKI, F.; VERLI, H.; FRAGOSO, R. R.; SCHROEDER, E. K.; CARLINI, C. R.; GROSSI-de-SÁ, M. F. |
|
Afiliação: |
FERNANDA MULINARI, UFRGS; ARLETE BEATRIZ BECKER-RITT, UFRGS; DIOGO RIBEIRO DEMARTINI, UFRGS; RODRIGO LIGABUE-BRAUN, UFRGS; FERNANDA STANISÇUASKI, UFRGS; HUGO VERLI, UFRGS; RODRIGO DA ROCHA FRAGOSO, CPAC; EVELYN KOECHE SCHROEDER, UFRGS; CÉLIA REGINA CARLINI, UFRGS; MARIA FATIMA GROSSI DE SA, CENARGEN. |
|
Título: |
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. |
|
Ano de publicação: |
2011 |
|
Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. |
|
Idioma: |
Inglês |
|
Conteúdo: |
Ureases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease isoform named JBURE-II, corresponding to a putative smaller urease protein (78 kDa) when compared to other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3? and 5? ends, encoding a 90 kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants. |
|
Thesagro: |
Canavalia Ensiformis. |
|
Categoria do assunto: |
-- |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/183508/1/1-s2.0-S1570963911002172-main.pdf
|
|
Marc: |
LEADER 02105naa a2200241 a 4500
001 1913253
005 2023-02-24
008 2011 bl uuuu u00u1 u #d
100 1 $aMULINARI, F.
245 $aCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.$h[electronic resource]
260 $c2011
520 $aUreases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease isoform named JBURE-II, corresponding to a putative smaller urease protein (78 kDa) when compared to other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3? and 5? ends, encoding a 90 kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants.
650 $aCanavalia Ensiformis
700 1 $aBECKER-RITT, A. B.
700 1 $aDEMARTINI, D. R.
700 1 $aLIGABUE-BRAUN, R.
700 1 $aSTANISÇUASKI, F.
700 1 $aVERLI, H.
700 1 $aFRAGOSO, R. R.
700 1 $aSCHROEDER, E. K.
700 1 $aCARLINI, C. R.
700 1 $aGROSSI-de-SÁ, M. F.
773 $tBiochimica et Biophysica Acta$gv. 1814, n. 12, p. 1758-1768, Dec. 2011.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
